The role of Phe150 in human voltage-gated proton channel.

ABSTRACT: The voltage-gated proton channel H_v1 is a member of voltage-gated ion channels containing voltage-sensing domains (VSDs). The VSDs are made of four membrane-spanning segments (S1 through S4), and their function is to detect changes in membrane potential in the cells. A highly conserved phenylalanine 150 (F150) is located in the S2 segment of human voltage-gated proton channels. We previously discovered that the F150 is a binding site for the open channel blocker 2GBI. Here, we show that the H_v1 VSD voltage-dependent activation requires a hydrophobic group at position F150. We perform double-mutant cycle analysis to probe interactions between F150 and positively charged arginines in the S4 segment of the channel. Our results indicate that F150 interacts with two argini

SUBMITTER: Wu X 

PROVIDER: S-EPMC9646954 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature